4ZWO
Crystal structure of organophosphate anhydrolase/prolidase mutant Y212F
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-BM |
Synchrotron site | APS |
Beamline | 22-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-10-16 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 103.391, 67.944, 140.450 |
Unit cell angles | 90.00, 110.08, 90.00 |
Refinement procedure
Resolution | 32.899 - 2.141 |
R-factor | 0.1736 |
Rwork | 0.172 |
R-free | 0.21170 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3l24 |
RMSD bond length | 0.003 |
RMSD bond angle | 0.619 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.9-1692) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.100 |
Rmerge | 0.075 |
Number of reflections | 49830 |
<I/σ(I)> | 18.8 |
Completeness [%] | 99.6 |
Redundancy | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | 4% PEG 4,000, 20% Isopropanol, 11 mM BaCl2 |